Effect of Various Glycosidase Treatments on the Resistance of the HIV-1 Envelope to Degradation

FEBS Lett. 1997 Apr 7;406(1-2):191-5. doi: 10.1016/s0014-5793(97)00273-1.

Abstract

Using a CD4-binding assay to assess the conformation of the human immunodeficiency virus envelope glycoprotein (CHO+ Env), we studied the effect of treatment with various glycosidases on the stability of Env in denaturing environments and in biological media: cleavage from Env of either high-mannose-type glycans (HMT- Env) by endoglycosidase H or sialic acid residues (Sial- Env) by sialidase did not alter Env stability whereas its complete deglycosylation (CHO- Env) by N-glycanase had a large effect. The influence of glycan removal on Env sensitivity to proteases was also studied. Thrombin cleavage within V3 was affected by N-glycanase treatment; both HMT- Env and CHO- Env displayed an increased sensitivity to other endoproteases. Thus, partial deglycosylation increases Env sensitivity to proteases but only its total deglycosylation alters its stability.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Blood
  • CD4 Antigens / metabolism
  • CHO Cells
  • Cricetinae
  • Gene Products, env / metabolism*
  • Glycoside Hydrolases / metabolism*
  • Glycosylation
  • Hydrolysis
  • Thrombin / metabolism

Substances

  • CD4 Antigens
  • Gene Products, env
  • Glycoside Hydrolases
  • Thrombin